The beta subunit of ATP synthase (encoded by atpD) is essential for catalytic ATP synthesis, utilizing proton gradients across membranes to phosphorylate ADP into ATP . In Acidiphilium cryptum, a bacterium thriving in acidic environments, this subunit enables energy production under extreme pH conditions. Recombinant versions allow targeted studies of ATP synthase mechanics and microbial adaptations .
Key properties of the recombinant protein include:
| Parameter | Details |
|---|---|
| UniProt ID | A5FZ54 |
| Source | Acidiphilium cryptum (strain JF-5) |
| Expression System | Escherichia coli |
| Purity | >85% (verified via SDS-PAGE) |
| Storage | -20°C (short-term); -80°C for long-term stability |
| Sequence Length | 474 amino acids (partial sequence provided below) |
Data derived from product specifications and peer-reviewed studies .
Catalytic Role: The beta subunit facilitates ATP synthesis by undergoing conformational changes during rotational catalysis, driven by proton motive force .
Evolutionary Conservation: Comparative genomic analyses reveal atpD as one of the least variable housekeeping genes in bacteria, underscoring its essential role in energy metabolism .
Research Applications: Recombinant atpD enables studies on ATP synthase inhibition, microbial energetics in extreme environments, and enzyme engineering for biotechnological uses .
Current data gaps include:
Structural Dynamics: High-resolution cryo-EM or crystallographic data for A. cryptum atpD remain unpublished.
Inhibitor Binding Studies: No reported investigations into small-molecule interactions with the recombinant protein.
Environmental Adaptations: Mechanistic links between atpD structure and acidophilic metabolism require further exploration .
KEGG: acr:Acry_1681
STRING: 349163.Acry_1681